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{
"metadata": {
"accession": "IPR000960",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0050660",
"name": "flavin adenine dinucleotide binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0050661",
"name": "NADP binding",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"pirsf": {
"PIRSF000332": "Dimethylaniline monooxygenase (N-oxide-forming)"
},
"prints": {
"PR00370": "FMOXYGENASE"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR020946",
"name": "Flavin monooxygenase-like",
"type": "Family",
"children": [
{
"accession": "IPR000960",
"name": "Flavin monooxygenase FMO",
"type": "Family",
"children": [
{
"accession": "IPR002253",
"name": "Flavin monooxygenase (FMO) 1",
"type": "Family",
"children": []
},
{
"accession": "IPR002254",
"name": "Flavin monooxygenase (FMO) 2",
"type": "Family",
"children": []
},
{
"accession": "IPR002255",
"name": "Flavin monooxygenase (FMO) 3",
"type": "Family",
"children": []
},
{
"accession": "IPR002256",
"name": "Flavin monooxygenase (FMO) 4",
"type": "Family",
"children": []
},
{
"accession": "IPR002257",
"name": "Flavin monooxygenase (FMO) 5",
"type": "Family",
"children": []
}
]
}
]
},
"name": {
"name": "Flavin monooxygenase FMO",
"short": "Flavin_mOase"
},
"description": [
{
"text": "<p>Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes [[cite:PUB00000158]]. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorus and selenium atoms in a range of structurally diverse compounds. FMOs have been implicated in the metabolism of a number of pharmaceuticals, pesticides and toxicants. In man, lack of hepatic FMO-catalysed trimethylamine metabolism results in trimethylaminuria (fish odour syndrome). Five mammalian forms of FMO are now known and have been designated FMO1-FMO5 [[cite:PUB00002642], [cite:PUB00002611], [cite:PUB00004772], [cite:PUB00000516], [cite:PUB00002834], [cite:PUB00101886]]. This is a recent nomenclature based on comparison of amino acid sequences, and has been introduced in an attempt to eliminate confusion inherent in multiple, laboratory-specific designations and tissue-based classifications [[cite:PUB00000158]]. Following the determination of the complete nucleotide sequence of Saccharomyces cerevisiae (Baker's yeast) [[cite:PUB00005185]], a novel gene was found to encode a protein with similarity to mammalian monooxygenases. In Aspergillus, flavin-containing monooxygenases ustF1 and ustF2 are components in the biosynthesis of the antimitotic tetrapeptide ustiloxin B, a secondary metabolite. The monooxygenases modify the side chain of the intermediate S-deoxyustiloxin H [[cite:PUB00082329]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00000158": {
"PMID": 8311461,
"ISBN": null,
"volume": "308",
"issue": "1",
"year": 1994,
"title": "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.",
"URL": null,
"raw_pages": "254-7",
"medline_journal": "Arch Biochem Biophys",
"ISO_journal": "Arch. Biochem. Biophys.",
"authors": [
"Lawton MP",
"Cashman JR",
"Cresteil T",
"Dolphin CT",
"Elfarra AA",
"Hines RN",
"Hodgson E",
"Kimura T",
"Ozols J",
"Phillips IR."
],
"DOI_URL": "http://dx.doi.org/10.1006/abbi.1994.1035"
},
"PUB00002642": {
"PMID": 1712018,
"ISBN": null,
"volume": "266",
"issue": "19",
"year": 1991,
"title": "Cloning, primary sequence, and chromosomal mapping of a human flavin-containing monooxygenase (FMO1).",
"URL": null,
"raw_pages": "12379-85",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Dolphin C",
"Shephard EA",
"Povey S",
"Palmer CN",
"Ziegler DM",
"Ayesh R",
"Smith RL",
"Phillips IR."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/266/19/12379"
},
"PUB00002611": {
"PMID": 2318837,
"ISBN": null,
"volume": "265",
"issue": "10",
"year": 1990,
"title": "The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes.",
"URL": null,
"raw_pages": "5855-61",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Lawton MP",
"Gasser R",
"Tynes RE",
"Hodgson E",
"Philpot RM."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/265/10/5855"
},
"PUB00004772": {
"PMID": 1542660,
"ISBN": null,
"volume": "89",
"issue": "5",
"year": 1992,
"title": "Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.",
"URL": null,
"raw_pages": "1685-9",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Lomri N",
"Gu Q",
"Cashman JR."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1542660&action=stream&blobtype=pdf"
},
"PUB00000516": {
"PMID": 1417778,
"ISBN": null,
"volume": "287 ( Pt 1)",
"issue": null,
"year": 1992,
"title": "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family.",
"URL": null,
"raw_pages": "261-7",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Dolphin CT",
"Shephard EA",
"Povey S",
"Smith RL",
"Phillips IR."
],
"DOI_URL": "http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1417778"
},
"PUB00002834": {
"PMID": 8486656,
"ISBN": null,
"volume": "268",
"issue": "13",
"year": 1993,
"title": "Cloning, sequencing, distribution, and expression in Escherichia coli of flavin-containing monooxygenase 1C1. Evidence for a third gene subfamily in rabbits.",
"URL": null,
"raw_pages": "9681-9",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Atta-Asafo-Adjei E",
"Lawton MP",
"Philpot RM."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/268/13/9681.pdf"
},
"PUB00005185": {
"PMID": 8091229,
"ISBN": null,
"volume": "265",
"issue": "5181",
"year": 1994,
"title": "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.",
"URL": null,
"raw_pages": "2077-82",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Johnston M",
"Andrews S",
"Brinkman R",
"Cooper J",
"Ding H",
"Dover J",
"Du Z",
"Favello A",
"Fulton L",
"Gattung S."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/265/5181/2077"
},
"PUB00082329": {
"PMID": 27166860,
"ISBN": null,
"volume": "55",
"issue": "28",
"year": 2016,
"title": "Unveiling the Biosynthetic Pathway of the Ribosomally Synthesized and Post-translationally Modified Peptide Ustiloxin B in Filamentous Fungi.",
"URL": null,
"raw_pages": "8072-5",
"medline_journal": "Angew Chem Int Ed Engl",
"ISO_journal": "Angew. Chem. Int. Ed. Engl.",
"authors": [
"Ye Y",
"Minami A",
"Igarashi Y",
"Izumikawa M",
"Umemura M",
"Nagano N",
"Machida M",
"Kawahara T",
"Shin-Ya K",
"Gomi K",
"Oikawa H."
],
"DOI_URL": "http://dx.doi.org/10.1002/anie.201602611"
},
"PUB00101886": {
"PMID": 32156684,
"ISBN": null,
"volume": "48",
"issue": "5",
"year": 2020,
"title": "Flavin-Containing Monooxygenase 1 Catalyzes the Production of Taurine from Hypotaurine.",
"URL": null,
"raw_pages": "378-385",
"medline_journal": "Drug Metab Dispos",
"ISO_journal": "Drug Metab Dispos",
"authors": [
"Veeravalli S",
"Phillips IR",
"Freire RT",
"Varshavi D",
"Everett JR",
"Shephard EA."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036188",
"name": "FAD/NAD(P)-binding domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 58420,
"pathways": 12,
"proteins": 31704,
"proteomes": 7067,
"sets": 0,
"structural_models": {
"alphafold": 26684,
"bfvd": 0
},
"structures": 40,
"taxa": 15177
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "1.14.13",
"url": "https://enzyme.expasy.org/EC/1.14.13"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "5nmx",
"name": "Crystal Structure of the pyrrolizidine alkaloid N-oxygenase from Zonocerus variegatus in complex with FAD and NADP+"
}
}
}
